Detalle de: Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus
| Title | Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus |
| Abstract |
Flavodoxins are small electron-transfer proteins that contain one molecule of noncovalently bound flavin mononucleotide (FMN). The flavodoxin NifF from the photosynthetic bacterium Rhodobacter capsulatus is reduced by one electron from ferredoxin/flavodoxin:NADP(H) reductase and was postulated to be an electron donor to nitrogenase in vivo. NifF was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of PEG 3350 and PEG 400 at pH 5.5 and belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 66.49, c = 121.32 A. X-ray data sets have been collected to 2.17 A resolution. |
| Apa Reference | Pérez-Dorado, I., Bortolotti, A., Cortez, N. & Hermoso, J.A. (2008). Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 64(5), 375-377. 10.1107/s1744309108008038 |
| Doi | 10.1107/s1744309108008038 |
| Publication Date | 5 Apr 2008 |
| Publication Type | Article |
| Researcher | Juana Inmaculada Pérez Dorado |
| Ontology | Model organisms |
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